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J Mol Biol. 2005 Oct 28;353(3):477-84. Epub 2005 Sep 9.

Histone H3 lysine 4 mono-methylation does not require ubiquitination of histone H2B.

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  • 1Laboratoire d'Ingénierie des Systèmes Macromoléculaires et Institut de Biologie Structurale et Microbiologie, CNRS, 31 chemin Joseph Aiguier, 13402, Marseille, Cedex 20, France.


The yeast Set1-complex catalyzes histone H3 lysine 4 (H3K4) methylation. Using N-terminal Edman sequencing, we determined that 50% of H3K4 is methylated and consists of roughly equal amounts of mono, di and tri-methylated H3K4. We further show that loss of either Paf1 of the Paf1 elongation complex, or ubiquitination of histone H2B, has only a modest effect on bulk histone mono-methylation at H3K4. Despite the fact that Set1 recruitment decreases in paf1delta cells, loss of Paf1 results in an increase of H3K4 mono-methylation at the 5' coding region of active genes, suggesting a Paf1-independent targeting of Set1. In contrast to Paf1 inactivation, deleting RTF1 affects H3K4 mono-methylation at the 3' coding region of active genes and results in a decrease of global H3K4 mono-methylation. Our results indicate that the requirements for mono-methylation are distinct from those for H3K4 di and tri-methylation, and point to differences among members of the Paf1 complex in the regulation of H3K4 methylation.

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